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Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

Journal of biotechnology, 2006-08, Vol.124 (4), p.670-689

2006

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Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications

Journal of biotechnology, 2010-03, Vol.146 (1), p.9-24

2010

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The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia

Critical reviews in oncology/hematology, 2004-05, Vol.50 (2), p.87-100

2004

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Effective redesign of oxidative enzymes for green chemistry—FP7 OXYGREEN

Journal of biotechnology, 2010-11, Vol.150, p.84-84

Fraaije, M.W.

2010

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From waste to value – direct utilization of limonene from orange peel in a biocatalytic cascade reaction towards chiral carvolactone

Green chemistry : an international journal and green chemistry resource : GC, 2017, Vol.19 (2), p.367-371

2017

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Identification of a novel oxygenase capable of regiospecific hydroxylation of d-limonene into (+)-trans-carveol

Tetrahedron, 2016-11, Vol.72 (46), p.7263-7267

2016

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Expanding the set of rhodococcal Baeyer–Villiger monooxygenases by high-throughput cloning, expression and substrate screening

Applied microbiology and biotechnology, 2012-09, Vol.95 (6), p.1479-1489

2012

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Multiple pathways guide oxygen diffusion into flavoenzyme active sites

Proceedings of the National Academy of Sciences - PNAS, 2009-06, Vol.106 (26), p.10603-10608

2009

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Optimizing monooxygenases for oxidative biocatalysis

New biotechnology, 2009-09, Vol.25, p.S127-S127

Fraaije, M.W.

2009

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Baeyer-Villiger Monooxygenases, an Emerging Family of Flavin-Dependent Biocatalysts

Advanced synthesis & catalysis, 2003-06, Vol.345 (6-7), p.667-678

2003

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The growing VAO flavoprotein family

Archives of biochemistry and biophysics, 2008-06, Vol.474 (2), p.292-301

2008

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The Oxidation of Thiols by Flavoprotein Oxidases: a Biocatalytic Route to Reactive Thiocarbonyls

Angewandte Chemie (International ed.), 2014-11, Vol.53 (48), p.13206-13209

International ed. in English, 2014

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Identification of a Gatekeeper Residue That Prevents Dehydrogenases from Acting as Oxidases

The Journal of biological chemistry, 2009-02, Vol.284 (7), p.4392-4397

2009

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Identification of a Baeyer–Villiger monooxygenase sequence motif

FEBS letters, 2002-05, Vol.518 (1), p.43-47

2002

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Elucidation of the 4-Hydroxyacetophenone Catabolic Pathway in Pseudomonas fluorescens ACB

Journal of Bacteriology, 2008-08, Vol.190 (15), p.5190-5198

2008

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Enzymatic Synthesis of Vanillin

Journal of agricultural and food chemistry, 2001-06, Vol.49 (6), p.2954-2958

2001

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Covalent Flavinylation Is Essential for Efficient Redox Catalysis in Vanillyl-alcohol Oxidase

The Journal of biological chemistry, 1999-12, Vol.274 (50), p.35514-35520

1999

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A novel oxidoreductase family sharing a conserved FAD-binding domain

Trends in biochemical sciences (Amsterdam. Regular ed.), 1998-06, Vol.23 (6), p.206-207

1998

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Structural Analysis of Flavinylation in Vanillyl-Alcohol Oxidase

The Journal of biological chemistry, 2000-12, Vol.275 (49), p.38654-38658

2000

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Flavoenzyme-Catalyzed Oxygenations and Oxidations of Phenolic Compounds

Advanced synthesis & catalysis, 2002-12, Vol.344 (10), p.1023-1035

2002

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Occurrence and Biocatalytic Potential of Carbohydrate Oxidases

Advances in Applied Microbiology, 2006, Vol.60, p.17-54

2006

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Inversion of Stereospecificity of Vanillyl-Alcohol Oxidase

Proceedings of the National Academy of Sciences - PNAS, 2000-08, Vol.97 (17), p.9455-9460

2000

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Regioselective dynamic kinetic resolution of alkyl indanones by novel Baeyer-Villiger monooxygenases

New biotechnology, 2009-09, Vol.25, p.S82-S83

2009

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Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase: evidence for formation of a p-quinone methide intermediate

The Journal of biological chemistry, 1997-07, Vol.272 (29), p.18111-18116

1997

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Hydroquinone dioxygenase from Pseudomonas fluorescens ACB: A novel member of the family of non-heme iron (II)-dependent dioxygenases

Journal of bacteriology, 2008, Vol.190

2008

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Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications

The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia

Effective redesign of oxidative enzymes for green chemistry—FP7 OXYGREEN

From waste to value – direct utilization of limonene from orange peel in a biocatalytic cascade reaction towards chiral carvolactone

Identification of a novel oxygenase capable of regiospecific hydroxylation of d-limonene into (+)-trans-carveol

Expanding the set of rhodococcal Baeyer–Villiger monooxygenases by high-throughput cloning, expression and substrate screening

Multiple pathways guide oxygen diffusion into flavoenzyme active sites

Optimizing monooxygenases for oxidative biocatalysis

Baeyer-Villiger Monooxygenases, an Emerging Family of Flavin-Dependent Biocatalysts

The growing VAO flavoprotein family

The Oxidation of Thiols by Flavoprotein Oxidases: a Biocatalytic Route to Reactive Thiocarbonyls

Identification of a Gatekeeper Residue That Prevents Dehydrogenases from Acting as Oxidases

Identification of a Baeyer–Villiger monooxygenase sequence motif

Elucidation of the 4-Hydroxyacetophenone Catabolic Pathway in Pseudomonas fluorescens ACB

Enzymatic Synthesis of Vanillin

Covalent Flavinylation Is Essential for Efficient Redox Catalysis in Vanillyl-alcohol Oxidase

A novel oxidoreductase family sharing a conserved FAD-binding domain

Structural Analysis of Flavinylation in Vanillyl-Alcohol Oxidase

Flavoenzyme-Catalyzed Oxygenations and Oxidations of Phenolic Compounds

Occurrence and Biocatalytic Potential of Carbohydrate Oxidases

Inversion of Stereospecificity of Vanillyl-Alcohol Oxidase

Regioselective dynamic kinetic resolution of alkyl indanones by novel Baeyer-Villiger monooxygenases

Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase: evidence for formation of a p-quinone methide intermediate

Hydroquinone dioxygenase from Pseudomonas fluorescens ACB: A novel member of the family of non-heme iron (II)-dependent dioxygenases

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